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Titolo:
Cloning and characterization of a novel human phosphatidylinositol transfer protein, rdgB beta
Autore:
Fullwood, Y; dos Santos, M; Hsuan, JJ;
Indirizzi:
Ludwig Inst Canc Res, London W1P 8BT, England Ludwig Inst Canc Res London England W1P 8BT Res, London W1P 8BT, England Univ Coll London, Royal Free & Univ Coll Med Sch, Dept Med, London NW3 2PF, England Univ Coll London London England NW3 2PF ept Med, London NW3 2PF, England
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 44, volume: 274, anno: 1999,
pagine: 31553 - 31558
SICI:
0021-9258(19991029)274:44<31553:CACOAN>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
RETINAL-DEGENERATION-B; CA2+-ACTIVATED SECRETION; DROSOPHILA-MELANOGASTER; GENE ENCODES; MUTANT; CELLS; PHOSPHORYLATION; MEMBRANE; HOMOLOG; ISOFORM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Hsuan, JJ Ludwig Inst Canc Res, Courtauld Bldg,91 Riding House St, London W1P 8BT, England Ludwig Inst Canc Res Courtauld Bldg,91 Riding House St London England W1P 8BT
Citazione:
Y. Fullwood et al., "Cloning and characterization of a novel human phosphatidylinositol transfer protein, rdgB beta", J BIOL CHEM, 274(44), 1999, pp. 31553-31558

Abstract

The various PITP, retinal degeneration B (rdgB), and amino-terminal domaininteracting receptor (Nir) phosphatidylinositol transfer proteins can be divided into two structural families. The small, soluble PITP isoforms contain only a phosphatidylinositol transfer domain and have been implicated in phosphoinositide signaling and vesicle trafficking. In contrast, the rdgB proteins, which include Nir2 and Nir3, contain an amino-terminal PITP-like domain, an acidic, Ca2+-binding domain, six putative transmembrane domains, and a conserved carboxyl-terminal domain. However, the biological function of rdgB proteins is unclear, Here, we report the isolation of a cDNA encoding a novel rdgB protein, mammalian rdgB beta (MrdgB beta). The 38-kDa MrdgBbeta protein contains an amino-terminal PITP-like domain and a short carboxyl-terminal domain. In contrast to other rdgB-like proteins, MrdgB beta contains no transmembrane motifs or the conserved carboxyl-terminal domain. Using Northern and reverse transcription-polymerase chain reaction analysis,we demonstrate that MrdgB beta mRNA is ubiquitously expressed. Immunofluorescence analysis of ectopic MrdgB beta showed cytoplasmic staining, and theability of recombinant MrdgB beta to transfer phosphatidylinositol in vitro was similar to other PITP-like domains. Although early reports found functional degeneracy in, vitro, the identification of a fifth mammalian PITP-like protein with a unique domain organization and widespread expression supports more recent results that suggest that different PITP-like domains have distinct functions in vivo.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 08:37:12